DIFFRACTION FROM CRYSTALS OF MULTIMODULE FIBRONECTIN CELL ADHESION FRAGMENTS

细胞表面受体对胞外配体的识别作用 (整合素)对细胞黏附、迁移和跟踪至关重要 也许是肿瘤细胞的转移性扩散。这一认可是 部分由精氨酸-甘氨酸-天冬氨酸序列介导 胞外蛋白。我们最近克隆并表达了更大的 每个都包含模块FN 11110的多模块片段。我们有 结晶了其中的三个碎片。这些碎片很重要 结构候选以揭示RGD场地的3D组织 以及相邻域中的协同站点，这是 整合素分子的识别和黏附功能。 需要同步辐射来收集来自这些卫星的重原子数据。 小晶体。

Recognition of extracellular ligands by cell surface receptors (integrins) is critical for cell adhesion, migration and tracking and perhaps the metastatic spread of tumor cells. This recognition is mediated in part by an arginine-glycine-aspartic acid sequence in extracellular proteins. We have recently cloned and expressed larger multimodule fragments that each contain the module FN 11110. We have crystallized three of these fragments. These fragments are important structural candidates to reveal the 3D organization of the RGD site and synergistic sites in adjacent domains that are required for integrin recognition and adhesive function of the molecule. Synchrotron radiation is needed to collect heavy atom data from these small crystals.